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Compositions and methods for preventing or treating cancer

Inactive Publication Date: 2005-12-22
UNIV OF NEBRASKA LINCOLN
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0005] One aspect of the present invention is a MUC1 cytoplasmic tail peptide of SEQ ID NO:1 or a portion thereof for preventing or treating cancer in a subject. In a preferred embodiment, the MUC1 cytoplasmic tail peptide of SEQ ID NO:1 is part of a vaccine.
[0006] Another aspe

Problems solved by technology

(1998) J. Gastroenterol. 33:354); however, these responses are ineffective at eliminating the tumors in vivo.
However, it has been shown that in vitro assays of cytolytic responses do not accurately predict MUC1-specific tumor rejection (Tempero, et al.

Method used

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Examples

Experimental program
Comparison scheme
Effect test

example 1

Cell Culture

[0040] The BL6 variant of the C57BL / 6-derived murine melanoma cell line B16 was maintained in Dulbecco's Minimal Essential Medium (DMEM) (GIBCO™ BRL, Div. of Life Technologies Inc., Rockville, Md.) supplemented with 10% heat-inactivated fetal bovine serum (BioWhittaker, Walkersville, Md.), essential amino acids (BioWhittaker), non-essential amino acids (Biowhittaker), sodium pyruvate (Sigma, St. Louis, Mo.), vitamins (GIBCO™), and penicillin / streptomycin (Biowhittaker). Panc02, a methylcholanthrene-induced pancreatic carcinoma syngeneic to C57BL / 6, was maintained in McCoy's 5A medium (GIBCO™) supplemented with 10% heat-inactivated fetal bovine serum, and penicillin / streptomycin in a humidified incubator at 37° C. and 5% CO2. EL4 cells were cultured in RPMI 1640 medium (GIBCO™) supplemented with 10% heat-inactivated fetal bovine serum and penicillin / streptomycin in a humidified incubator at 37° C. and 5% CO2. Culture media for MUC1 transfectant clones of B16, Panc02 and ...

example 2

Expression of Epitope-Tagged MUC1 Deletion Constructs

[0041] B16 and Panc02 were transfected with plasmid DNA encoding a full-length human MUC1 cDNA (B16.MUC1 or Panc02.MUC1) or control expression vector (B16.neo, or Panc02.neo) as has been described (Rowse, et al. (1998) supra; Morikane, et al. (1999) supra). The full-length cytoplasmic tail was 69 amino acids in length. MUC1 cytoplasmic tail deletion constructs were generated using well-established methods (Pemberton, et al. (1996) J. Biol. Chem. 271:2332; Burdick, et al. (1997) J. Biol. Chem. 272:24198). The tandem repeat was comprised of a 20 amino acid sequence (Pro-Asp-Thr-Arg-Pro-Ala-Pro-Gly-Ser-Thr-Ala-Pro-Pro-Ala-His-Gly-Val-Thr-Ser-Ala; SEQ ID NO:50) that repeated 42 times. The MUC1 tandem repeat deleted (ΔTR) construct was generated using well-known methods (Pemberton, et al. (1996) supra; Burdick, et al. (1997) supra). FLAG® epitope-tagged human MUC1 cDNA constructs in which portions of the cytoplasmic tail (MUC1.CT3, MU...

example 3

Preparation of Cell Lysates

[0042] Cell lysates were prepared by scraping cells into 1 mL of lysis buffer (10 mM Tris, 150 mM NaCl, 1 mM phenylmethylsulfonyl fluoride, 1% TRITON® X-100) with a rubber cell scraper. Lysates were incubated on ice, for 30 minutes and centrifuged at 4° C. for two minutes at 6,000 rpm to remove cell debris. Supernatants were transferred to fresh tubes and protein content was determined using the BTO-RAD® protein assay (BIO-RAD®, Hercules, Calif.) with bovine serum albumin standards. Cell lysates were stored at −20° C.

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Abstract

The present invention relates to a MUC1 cytoplasmic tail peptide or portion thereof. These peptides are useful for inducing an immune response to MUC1-expressing tumor cells and thus for preventing or treating cancer.

Description

INTRODUCTION [0001] This invention was made in the course of research sponsored by the National Institutes of Health (NIH Grant Nos. CA72712, CA57362 CA09476). The U.S. government may have certain rights in this invention.BACKGROUND OF THE INVENTION [0002] MUC1 is a large, transmembrane glycoprotein expressed on the apical surface of many types of polarized epithelia including pancreas, lung, breast and the gastrointestinal tract (Finn, et al. (1995) Immunol. Rev. 145:61). MUC1 is overexpressed and differentially glycosylated by a number of adenocarcinomas (Croce, et al. (1997) Anticancer Res. 17:4287) and has been evaluated as a candidate antigen for active immunotherapy protocols. Humoral and cell-mediated immune responses against MUC1 are detected in patients with MUC1+ tumors, as measured in vitro (Domenech, et al. (1995) J. Immunol. 155:4766; Petrarca, et al. (1999) Cancer Immunol. Immunother. 47:272; Nakamura, et al. (1998) J. Gastroenterol. 33:354); however, these responses a...

Claims

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Application Information

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IPC IPC(8): A61K38/17
CPCA61K38/1709A61P35/00A61P35/04
Inventor HOLLINGSWORTH, TONYKOHLGRAF, KARLCAFFREY, TOM
Owner UNIV OF NEBRASKA LINCOLN
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